Expression analysis of the entire MMP and TIMP gene families during mouse tissue development

FEBS Letters

Nuttall, Robert K¹  Sampieri, Clara L¹  Edwards, Dylan R¹  Schultz, Gilbert A²  Pennington, Caroline J¹  Gill, Sean E³ 

[1] School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK;Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, AB, Canada T2N 4N1;Department of Physiology and Pharmacology, University of Western Ontario, London, ON, Canada N6A 5C1

关键词: Matrix metalloproteinase;    Adamalysin;    Tissue inhibitor of metalloproteinase;    Mouse tissue development;    Real-time polymerase chain reaction;    MP;    metalloproteinase;    MMP;    matrix metalloproteinase;    TIMP;    tissue inhibitor of metalloproteinase;    ADAM;    a disintegrin and metalloproteinase;    or adamalysin;    pc;    post coitum;    qPCR;    quantitative real-time polymerase chain reaction;    C T;    cycle threshold;    GPI;    glycosylphosphatidylinositol;   

DOI  :  10.1016/S0014-5793(04)00281-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Matrix metalloproteinases (MMPs) and adamalysins (ADAMs) cleave many extracellular proteins, including matrix, growth factors, and receptors. We profiled the RNA levels of every MMP, several ADAMs, and inhibitors of metalloproteinases (TIMPs and RECK) in numerous mouse tissues during development and in the uterus during pregnancy. Observations include: most secreted MMPs are expressed at low to undetectable levels in tissues, whereas membrane-bound MMPs, ADAMs and inhibitors are abundant; almost every proteinase and inhibitor is present in the uterus or placenta at some time during gestation; the mouse collagenases mColA and mColB are found exclusively in the uterus and testis; and each tissue has its unique signature of proteinase and inhibitor expression.

【 授权许可】

Unknown